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Protein

Guanine nucleotide-binding protein G(s) subunit alpha isoforms short

Gene

GNAS

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP (PubMed:2022671, PubMed:9395396, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). GNAS functions downstream of several GPCRs, including beta-adrenergic receptors. Stimulates the Ras signaling pathway via RAPGEF2 (By similarity).By similarity3 Publications3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi54Magnesium1 Publication6 Publications1
Metal bindingi204Magnesium1 Publication6 Publications1
Binding sitei366GTP; via amide nitrogen7 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi47 – 55GTP7 Publications9
Nucleotide bindingi197 – 204GTP7 Publications8
Nucleotide bindingi223 – 227GTP7 Publications5
Nucleotide bindingi292 – 295GTP7 Publications4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Alternative name(s):
Adenylate cyclase-stimulating G alpha protein
Gene namesi
Name:GNAS
Synonyms:GNAS1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cell membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002037171 – 394Guanine nucleotide-binding protein G(s) subunit alpha isoforms shortAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-palmitoyl glycine1 Publication1
Lipidationi3S-palmitoyl cysteine1 Publication1
Cross-linki300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei352PhosphoserineBy similarity1

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP04896.
PRIDEiP04896.

PTM databases

SwissPalmiP04896.

Expressioni

Gene expression databases

BgeeiENSBTAG00000017475.

Interactioni

Subunit structurei

Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (PubMed:9395396, PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Interacts with CRY1; the interaction may block GPCR-mediated regulation of cAMP concentrations. Interacts with ADCY6 and stimulates its adenylyl cyclase activity (By similarity). Interacts with ADCY2 and ADCY5 (PubMed:9395396, PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Stimulates the ADCY5 adenylyl cyclase activity (By similarity).By similarity7 Publications

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-588N.
IntActiP04896. 1 interactor.
STRINGi9913.ENSBTAP00000023246.

Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 39Combined sources4
Beta strandi40 – 48Combined sources9
Helixi53 – 64Combined sources12
Helixi87 – 89Combined sources3
Helixi90 – 112Combined sources23
Beta strandi113 – 115Combined sources3
Helixi122 – 124Combined sources3
Helixi125 – 133Combined sources9
Turni134 – 136Combined sources3
Helixi144 – 155Combined sources12
Helixi157 – 163Combined sources7
Helixi164 – 168Combined sources5
Helixi175 – 179Combined sources5
Helixi182 – 185Combined sources4
Beta strandi187 – 189Combined sources3
Helixi194 – 199Combined sources6
Beta strandi206 – 214Combined sources9
Beta strandi217 – 224Combined sources8
Helixi228 – 237Combined sources10
Turni238 – 240Combined sources3
Beta strandi243 – 249Combined sources7
Helixi252 – 254Combined sources3
Turni258 – 260Combined sources3
Beta strandi261 – 264Combined sources4
Helixi265 – 277Combined sources13
Helixi280 – 282Combined sources3
Beta strandi283 – 285Combined sources3
Beta strandi287 – 292Combined sources6
Helixi294 – 303Combined sources10
Helixi308 – 310Combined sources3
Helixi313 – 316Combined sources4
Helixi332 – 350Combined sources19
Turni354 – 356Combined sources3
Beta strandi359 – 363Combined sources5
Beta strandi365 – 367Combined sources3
Helixi369 – 392Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZSX-ray2.30C1-394[»]
1AZTX-ray2.30A/B1-394[»]
1CJKX-ray3.00C1-394[»]
1CJTX-ray2.80C1-394[»]
1CJUX-ray2.80C1-394[»]
1CJVX-ray3.00C1-394[»]
1CS4X-ray2.50C1-394[»]
1CULX-ray2.40C1-394[»]
1TL7X-ray2.80C1-394[»]
1U0HX-ray2.90C1-394[»]
2GVDX-ray2.90C1-394[»]
2GVZX-ray3.27C1-394[»]
3C14X-ray2.68C1-394[»]
3C15X-ray2.78C1-394[»]
3C16X-ray2.87C1-394[»]
3G82X-ray3.11C1-394[»]
3MAAX-ray3.00C1-394[»]
3SN6X-ray3.20A1-394[»]
ProteinModelPortaliP04896.
SMRiP04896.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04896.

Family & Domainsi

Sequence similaritiesi

Belongs to the G-alpha family. G(s) subfamily.Curated

Phylogenomic databases

eggNOGiKOG0099. Eukaryota.
ENOG410XPC4. LUCA.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP04896.
KOiK04632.

Family and domain databases

CDDicd00066. G-alpha. 1 hit.
Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000367. Gprotein_alpha_S.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 2 hits.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00443. GPROTEINAS.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Gnas-1 (identifier: P04896-1) [UniParc]FASTAAdd to basket
Also known as: Alpha-S2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE
60 70 80 90 100
SGKSTIVKQM RILHVNGFNG EGGEEDPQAA RSNSDGEKAT KVQDIKNNLK
110 120 130 140 150
EAIETIVAAM SNLVPPVELA NPENQFRVDY ILSVMNVPDF DFPPEFYEHA
160 170 180 190 200
KALWEDEGVR ACYERSNEYQ LIDCAQYFLD KIDVIKQDDY VPSDQDLLRC
210 220 230 240 250
RVLTSGIFET KFQVDKVNFH MFDVGGQRDE RRKWIQCFND VTAIIFVVAS
260 270 280 290 300
SSYNMVIRED NQTNRLQEAL NLFKSIWNNR WLRTISVILF LNKQDLLAEK
310 320 330 340 350
VLAGKSKIED YFPEFARYTT PEDATPEPGE DPRVTRAKYF IRDEFLRIST
360 370 380 390
ASGDGRHYCY PHFTCAVDTE NIRRVFNDCR DIIQRMHLRQ YELL
Length:394
Mass (Da):45,709
Last modified:August 13, 1987 - v1
Checksum:i4D07A734AFF2A6BC
GO
Isoform Gnas-2 (identifier: P04896-2) [UniParc]FASTAAdd to basket
Also known as: Alpha-S1

The sequence of this isoform differs from the canonical sequence as follows:
     71-84: Missing.

Show »
Length:380
Mass (Da):44,280
Checksum:i5B06C75B1A366920
GO
Isoform Nesp55 (identifier: O18979-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry O18979.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Shares no sequence similarity with other isoforms due to a novel first exon containing the entire reading frame spliced to shared exon 2 so that exons 2-13 make up the 3'-UTR.
Length:241
Mass (Da):27,494
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18A → G in AAA30560 (PubMed:3081893).Curated1
Sequence conflicti85D → S in AAA30560 (PubMed:3081893).Curated1
Sequence conflicti363F → S in AAA30560 (PubMed:3081893).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00183271 – 84Missing in isoform Gnas-2. CuratedAdd BLAST14

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03404 mRNA. Translation: CAA27137.1.
M13006 mRNA. Translation: AAA30560.1.
BC102905 mRNA. Translation: AAI02906.1.
BC122757 mRNA. Translation: AAI22758.1.
M14014 mRNA. Translation: AAA30557.1.
PIRiA23818. RGBOGA.
I45904.
RefSeqiNP_001258700.1. NM_001271771.1.
NP_851364.1. NM_181021.3. [P04896-1]
UniGeneiBt.64619.
Bt.91987.

Genome annotation databases

GeneIDi281793.
KEGGibta:281793.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03404 mRNA. Translation: CAA27137.1.
M13006 mRNA. Translation: AAA30560.1.
BC102905 mRNA. Translation: AAI02906.1.
BC122757 mRNA. Translation: AAI22758.1.
M14014 mRNA. Translation: AAA30557.1.
PIRiA23818. RGBOGA.
I45904.
RefSeqiNP_001258700.1. NM_001271771.1.
NP_851364.1. NM_181021.3. [P04896-1]
UniGeneiBt.64619.
Bt.91987.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZSX-ray2.30C1-394[»]
1AZTX-ray2.30A/B1-394[»]
1CJKX-ray3.00C1-394[»]
1CJTX-ray2.80C1-394[»]
1CJUX-ray2.80C1-394[»]
1CJVX-ray3.00C1-394[»]
1CS4X-ray2.50C1-394[»]
1CULX-ray2.40C1-394[»]
1TL7X-ray2.80C1-394[»]
1U0HX-ray2.90C1-394[»]
2GVDX-ray2.90C1-394[»]
2GVZX-ray3.27C1-394[»]
3C14X-ray2.68C1-394[»]
3C15X-ray2.78C1-394[»]
3C16X-ray2.87C1-394[»]
3G82X-ray3.11C1-394[»]
3MAAX-ray3.00C1-394[»]
3SN6X-ray3.20A1-394[»]
ProteinModelPortaliP04896.
SMRiP04896.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-588N.
IntActiP04896. 1 interactor.
STRINGi9913.ENSBTAP00000023246.

PTM databases

SwissPalmiP04896.

Proteomic databases

PaxDbiP04896.
PRIDEiP04896.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281793.
KEGGibta:281793.

Organism-specific databases

CTDi2778.

Phylogenomic databases

eggNOGiKOG0099. Eukaryota.
ENOG410XPC4. LUCA.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP04896.
KOiK04632.

Miscellaneous databases

EvolutionaryTraceiP04896.

Gene expression databases

BgeeiENSBTAG00000017475.

Family and domain databases

CDDicd00066. G-alpha. 1 hit.
Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000367. Gprotein_alpha_S.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 2 hits.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00443. GPROTEINAS.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiGNAS2_BOVIN
AccessioniPrimary (citable) accession number: P04896
Secondary accession number(s): Q0II85, Q3SZE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 30, 2016
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The GNAS locus is imprinted in a complex manner, giving rise to distinct paternally, maternally and biallelically expressed proteins.
Crystal structures were determined for GNAS in complex with an adenylyl cyclase catalytic domain that was reconstructed from ADCY2 and ADCY5 N- and C-terminal domains.7 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.